Journal
INTERNATIONAL JOURNAL OF FOOD SCIENCE AND TECHNOLOGY
Volume 51, Issue 12, Pages 2621-2629Publisher
WILEY-BLACKWELL
DOI: 10.1111/ijfs.13248
Keywords
Amyloid nanofibrils; hydrophobic interaction; self-assemble; -zein
Categories
Funding
- National Key Technology R&D Program of Chinese Ministry of Science and Technology [2015BAD14B06]
- National Natural Science Foundation of China [21474125, 51608509]
- Shandong Collaborative Innovation Center for marine biomass fibre materials and textiles and Chinese '1000 youth Talent Program'
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Protein fibrillation serves a broad range of biological functions from surface colonising to mechanically reinforcing structures; it is also associated with the development of neurodegenerative disorders. Although fibrillation is considered to be an inherent ability of polypeptides to form backbones, relevant studies have long concentrated on aqueous-soluble proteins rather than on insoluble structures. In this study, the self-assembly of hydrophobic proteins into amyloid nanofibrils was studied using -zein as a model protein. The self-assembled morphologies of -zein were determined by hydrophobic-hydrophilic characters of both the protein and the solvent. Upon thermally incubating in aqueous ethanol, -zein formed amyloid nanofibrils with lower ethanol compositions and near-neutral pHs, while acidic conditions and high ethanol compositions result in the formation of spherical aggregations. The fibrillation of -zein shows a great potential in serving as bio-based gels or reinforced fillers in food, cosmetic and pharmaceutical applications.
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